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目的探讨沙门菌毒力效应蛋白Sse L对不同连接方式连接泛素链的水解特异性。方法克隆伤寒沙门菌Ty2菌株Sse L基因,融合表达纯化GST-Sse L蛋白并在体外研究其对Ub-AMC及各种泛素链的水解情况。结果 Sse L对Ub-AMC水解活性很低,对直链泛素基本没有活性;而对K48和K63连接的二泛素表现出很高的水解活性。结论沙门菌毒力效应蛋白Sse L具有特异性水解泛素异肽链活性,并且对K63多聚泛素链具有更高地水解活性。
Objective To investigate the hydrolytic specificity of Salmonella virulence-effect protein Sse L on the ligation of ubiquitin chains by different ligation methods. Methods The Sse L gene of Salmonella Typhi Ty2 was cloned and the GST-Sse L protein was purified by fusion and the hydrolysis of Ub-AMC and various ubiquitin chains was studied in vitro. Results Sse L had low activity on Ub-AMC and little activity on straight-chain ubiquitin. However, Ubiquitin linked to K48 and K63 showed high hydrolytic activity. Conclusion Salmonella typhimurium virulence factor Sse L has specific hydrolytic ubiquitin isopeptide chain activity and higher hydrolysis activity to K63 polyubiquitin chains.